title: Comparative phenotypic analysis of articular chondrocytes cultured within type I or type II collagen scaffolds.
abstract: Among the existing repair strategies for cartilage injury, tissue engineering approach using biomaterials and chondrocytes offers hope for treatments. In this context, collagen-based biomaterials are good candidates as scaffolds for chondrocytes in cell transplantation procedures. These scaffolds are provided under different forms (gel or crosslinked sponge) made with either type I collagen or type I or type II atelocollagen molecules. The present study was undertaken to investigate how bovine articular chondrocytes sense and respond to differences in the structure and organization of these collagen scaffolds, over a 12-day culture period. When chondrocytes were seeded in the collagen scaffolds maintained in free-floating conditions, cells contracted gels to 40-60% and sponges to 15% of their original diameter. Real-time polymerase chain reaction analysis indicated that the chondrocyte phenotype, assessed notably by the ratio of COL2A1/COL1A2 mRNA and alpha10/alpha11 integrin subunit mRNA, was comparatively better sustained in type I collagen sponges when seeded at high cell density, also in type I atelocollagen gels. Besides, proteoglycan accumulation in the different scaffolds, as assessed by measuring the sulfated glycosaminoglycan content, was found be highest in type I collagen sponges seeded at high cell density. In addition, gene expression of matrix metalloproteinase-13 increased dramatically (up to 90-fold) in chondrocytes cultured in the different gels, whereas it remained stable in the sponges. Our data taken together reveal that type I collagen sponges seeded at high cell density represent a suitable material for tissue engineering of cartilage.
authors.affiliation: Institut de Biologie et Chimie des Protéines, CNRS UMR 5086, Université de Lyon, IFR 128, Lyon, France. am.freyria@ibcp.fr
authors.forename: Anne-Marie
authors.initials: AM
authors.lastname: Freyria
authors.forename: Marie-Claire
authors.initials: MC
authors.lastname: Ronzière
authors.forename: Delphine
authors.initials: D
authors.lastname: Cortial
authors.forename: Laurent
authors.initials: L
authors.lastname: Galois
authors.forename: Daniel
authors.initials: D
authors.lastname: Hartmann
authors.forename: Daniel
authors.initials: D
authors.lastname: Herbage
authors.forename: Frédéric
authors.initials: F
authors.lastname: Mallein-Gerin
mesh_terms: D053674:Aggrecans / Q000378:metabolism; D000818:Animals; D001672:Biocompatible Materials / Q000378:metabolism; D015415:Biomarkers / Q000378:metabolism; D002358:Cartilage, Articular / Q000166:cytology*; D002417:Cattle; D054337:Cell Dedifferentiation / Q000187:drug effects; D002454:Cell Differentiation / Q000187:drug effects; D049109:Cell Proliferation / Q000187:drug effects; D048430:Cell Shape / Q000187:drug effects; D002478:Cells, Cultured; D019902:Chondrocytes / Q000166:cytology* / Q000187:drug effects* / Q000201:enzymology; D024042:Collagen Type I / Q000494:pharmacology* / Q000648:ultrastructure; D024043:Collagen Type II / Q000494:pharmacology* / Q000648:ultrastructure; D016326:Extracellular Matrix Proteins / Q000235:genetics / Q000378:metabolism; D005782:Gels; D005786:Gene Expression Regulation / Q000187:drug effects; D020781:Matrix Metalloproteinase 1 / Q000235:genetics / Q000378:metabolism; D053509:Matrix Metalloproteinase 13 / Q000235:genetics / Q000378:metabolism; D010641:Phenotype; D054457:Tissue Scaffolds / Q000737:chemistry*
chemical_list: D053674:Aggrecans; D001672:Biocompatible Materials; D015415:Biomarkers; D024042:Collagen Type I; D024043:Collagen Type II; D016326:Extracellular Matrix Proteins; D005782:Gels; D053509:Matrix Metalloproteinase 13; D020781:Matrix Metalloproteinase 1